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Date of Award
Restricted Thesis: Campus only access
Bachelor of Science
Dr. Linda Boland
Potassium two-pore domain (K2P) channels play an important role in the regulation of the resting membrane potential and electrical signaling. Among the subfamilies of K2P, there is a lack of conservation of the C-terminal sequence, supporting the idea that the unique sensitivity of each K2P subfamily is based in the C-terminus. The TREK subfamily is activated by alkaline pH, fatty acids, membrane stretch, and phosphorylation. Previous studies have characterized regions of the C-terminus in their role of responding to these stimuli. Using Xenopus oocyte expression in conjunction with chemiluminescence techniques, we aimed to investigate the role of regions of the TREK-1 C-terminus in regulation of sensitivity to a fatty acid. Chemiluminescence assays of epitope-tagged TREK-1 C-terminal mutants suggest that the region between G308 and L332 is critical for channel expression. Whole cell recordings suggest that the proximal region of the C-terminus plays a role in activation by arachidonic acid (AA). In trying to connect these critical regions to previously-characterized regions, we are moving toward investigating the overlapping roles of AKAP scaffolding proteins and GRK phosphorylation in activation of TREK by AA.
Heine, Bridgette, "Characterizing the role of the C-terminus of a potassium ion channel" (2017). Honors Theses. 998.